We show here that PrPC, the normal isoform of the prion protein (PrPSc), co
uld be retained by a Cu2+-loaded resin through two different binding sites.
Contrarily, PrPSc was not retained at all by such resin. This constitutes
a new prion-specific property of PrPSc, which in addition to protease resis
tance and beta -sheet content, may result from its aberrant conformation.